当前位置:
X-MOL 学术
›
Nat. Catal.
›
论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Nitrogenase loosens its belt to fix dinitrogen
Nature Catalysis ( IF 37.8 ) Pub Date : 2022-05-25 , DOI: 10.1038/s41929-022-00795-2 Ross D. Milton
Nature Catalysis ( IF 37.8 ) Pub Date : 2022-05-25 , DOI: 10.1038/s41929-022-00795-2 Ross D. Milton
Nitrogenase reduces dinitrogen at one of its iron–sulfur cores to produce ammonia by a convoluted mechanism. Now, research highlights the importance of sulfur mobility on one of nitrogenase’s metallocofactors for nitrogen fixation.
中文翻译:
固氮酶松带固定二氮
固氮酶通过复杂的机制在其铁硫核心之一还原二氮以产生氨。现在,研究强调了硫迁移性对固氮酶的一种金属因子固氮的重要性。
更新日期:2022-05-26
中文翻译:
固氮酶松带固定二氮
固氮酶通过复杂的机制在其铁硫核心之一还原二氮以产生氨。现在,研究强调了硫迁移性对固氮酶的一种金属因子固氮的重要性。